Peptide-functionalized spherical polyelectrolyte nanobrushes for real-time sensing of protease activity

Bin Cheng Yin; Min Zhang; Weihong Tan; Bang Ce Ye

doi:10.1002/cbic.200900735

Peptide-functionalized spherical polyelectrolyte nanobrushes for real-time sensing of protease activity

Bin Cheng Yin, Min Zhang, Weihong Tan^*, Bang Ce Ye

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

(Figure Presented) Magic nanobrush: We report an effective self-assembled spherical polyelectrolyte nanobrush (SPB) composites with peptides and demonstrate its feasibility in detecting protease activity in a homogeneous solution. This assay allows rapid and accurate determination of protease kinetic parameters as well as inhibition constants. The sensitivity can be significantly improved to 1.0 x 10^-3 units (1.85-5.55 nm) thrombin. Our results demonstrate that SPBs, as a new class of nanostructures, can provide an excellent platform for enzyme studies and molecular sensing development.

Original language	English
Pages (from-to)	494-497
Number of pages	4
Journal	ChemBioChem
Volume	11
Issue number	4
DOIs	https://doi.org/10.1002/cbic.200900735
State	Published - 1 Mar 2010
Externally published	Yes

Keywords

Fluorescence polarization
Fluorescent probes
Inhibitors
Proteases
Thrombin

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10.1002/cbic.200900735

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title = "Peptide-functionalized spherical polyelectrolyte nanobrushes for real-time sensing of protease activity",

abstract = "(Figure Presented) Magic nanobrush: We report an effective self-assembled spherical polyelectrolyte nanobrush (SPB) composites with peptides and demonstrate its feasibility in detecting protease activity in a homogeneous solution. This assay allows rapid and accurate determination of protease kinetic parameters as well as inhibition constants. The sensitivity can be significantly improved to 1.0 x 10-3 units (1.85-5.55 nm) thrombin. Our results demonstrate that SPBs, as a new class of nanostructures, can provide an excellent platform for enzyme studies and molecular sensing development.",

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author = "Yin, \{Bin Cheng\} and Min Zhang and Weihong Tan and Ye, \{Bang Ce\}",

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doi = "10.1002/cbic.200900735",

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T1 - Peptide-functionalized spherical polyelectrolyte nanobrushes for real-time sensing of protease activity

AU - Yin, Bin Cheng

AU - Zhang, Min

AU - Tan, Weihong

AU - Ye, Bang Ce

PY - 2010/3/1

Y1 - 2010/3/1

N2 - (Figure Presented) Magic nanobrush: We report an effective self-assembled spherical polyelectrolyte nanobrush (SPB) composites with peptides and demonstrate its feasibility in detecting protease activity in a homogeneous solution. This assay allows rapid and accurate determination of protease kinetic parameters as well as inhibition constants. The sensitivity can be significantly improved to 1.0 x 10-3 units (1.85-5.55 nm) thrombin. Our results demonstrate that SPBs, as a new class of nanostructures, can provide an excellent platform for enzyme studies and molecular sensing development.

AB - (Figure Presented) Magic nanobrush: We report an effective self-assembled spherical polyelectrolyte nanobrush (SPB) composites with peptides and demonstrate its feasibility in detecting protease activity in a homogeneous solution. This assay allows rapid and accurate determination of protease kinetic parameters as well as inhibition constants. The sensitivity can be significantly improved to 1.0 x 10-3 units (1.85-5.55 nm) thrombin. Our results demonstrate that SPBs, as a new class of nanostructures, can provide an excellent platform for enzyme studies and molecular sensing development.

KW - Fluorescence polarization

KW - Fluorescent probes

KW - Inhibitors

KW - Proteases

KW - Thrombin

UR - https://www.scopus.com/pages/publications/77149163344

U2 - 10.1002/cbic.200900735

DO - 10.1002/cbic.200900735

M3 - 文章

C2 - 20112322

AN - SCOPUS:77149163344

SN - 1439-4227

VL - 11

SP - 494

EP - 497

JO - ChemBioChem

JF - ChemBioChem

IS - 4

ER -

Peptide-functionalized spherical polyelectrolyte nanobrushes for real-time sensing of protease activity

Abstract

Keywords

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